ID A1VTK1_POLNA Unreviewed; 730 AA. AC A1VTK1; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 02-SEP-2026, entry version 124. DE RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|NCBIfam:TIGR01345}; DE EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|NCBIfam:TIGR01345}; GN Name=glcB {ECO:0000256|HAMAP-Rule:MF_00641}; GN OrderedLocusNames=Pnap_3683 {ECO:0000313|EMBL:ABM38979.1}; OS Polaromonas naphthalenivorans (strain CJ2). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Comamonadaceae; Polaromonas. OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM38979.1, ECO:0000313|Proteomes:UP000000644}; RN [1] {ECO:0000313|Proteomes:UP000000644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644}; RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x; RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.; RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal RT tar-contaminated sediment, reveals physiological and metabolic versatility RT and evolution through extensive horizontal gene transfer."; RL Environ. Microbiol. 11:2253-2270(2009). CC -!- FUNCTION: Involved in the glycolate utilization. Catalyzes the CC condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CC CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP- CC Rule:MF_00641}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glyoxylate + acetyl-CoA + H2O = (S)-malate + CoA + H(+); CC Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00641, ECO:0000256|RuleBase:RU003572}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP- CC Rule:MF_00641}; CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from CC isocitrate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00641, CC ECO:0000256|RuleBase:RU003572}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00641}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641, CC ECO:0000256|RuleBase:RU003572}. CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00641}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000529; ABM38979.1; -; Genomic_DNA. DR RefSeq; WP_011803045.1; NC_008781.1. DR AlphaFoldDB; A1VTK1; -. DR STRING; 365044.Pnap_3683; -. DR KEGG; pna:Pnap_3683; -. DR eggNOG; COG2225; Bacteria. DR HOGENOM; CLU_028446_1_0_4; -. DR OrthoDB; 9762054at2; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000000644; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter. DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009436; P:glyoxylate catabolic process; IEA:TreeGrafter. DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule. DR CDD; cd00728; malate_synt_G; 1. DR FunFam; 3.20.20.360:FF:000003; Malate synthase G; 1. DR Gene3D; 3.20.20.360; Malate synthase, domain 3; 2. DR Gene3D; 1.20.1220.12; Malate synthase, domain III; 1. DR HAMAP; MF_00641; Malate_synth_G; 1. DR InterPro; IPR044856; Malate_synth_C_sf. DR InterPro; IPR011076; Malate_synth_sf. DR InterPro; IPR001465; Malate_synthase_TIM. DR InterPro; IPR006253; Malate_synthG. DR InterPro; IPR048355; MS_C. DR InterPro; IPR048356; MS_N. DR InterPro; IPR046363; MS_N_TIM-barrel_dom. DR InterPro; IPR048357; MSG_insertion. DR NCBIfam; TIGR01345; malate_syn_G; 1. DR NCBIfam; NF002825; PRK02999.1; 1. DR PANTHER; PTHR42739; MALATE SYNTHASE G; 1. DR PANTHER; PTHR42739:SF1; MALATE SYNTHASE G; 1. DR Pfam; PF20659; MS_C; 1. DR Pfam; PF20656; MS_N; 1. DR Pfam; PF01274; MS_TIM-barrel; 1. DR Pfam; PF20658; MSG_insertion; 1. DR SUPFAM; SSF51645; Malate synthase G; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:ABM38979.1}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00641}; KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435, ECO:0000256|HAMAP- KW Rule:MF_00641}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00641}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00641}; KW Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|HAMAP-Rule:MF_00641}; KW Reference proteome {ECO:0000313|Proteomes:UP000000644}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00641}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP- KW Rule:MF_00641}. FT DOMAIN 16..76 FT /note="Malate synthase N-terminal" FT /evidence="ECO:0000259|Pfam:PF20656" FT DOMAIN 160..234 FT /note="Malate synthase G alpha-beta insertion" FT /evidence="ECO:0000259|Pfam:PF20658" FT DOMAIN 336..573 FT /note="Malate synthase TIM barrel" FT /evidence="ECO:0000259|Pfam:PF01274" FT DOMAIN 597..694 FT /note="Malate synthase C-terminal" FT /evidence="ECO:0000259|Pfam:PF20659" FT ACT_SITE 339 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641, FT ECO:0000256|PIRSR:PIRSR601465-50" FT ACT_SITE 637 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641, FT ECO:0000256|PIRSR:PIRSR601465-50" FT BINDING 118 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 125..126 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 275 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 312 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 339 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 433 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 433 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 458..461 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 461 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 542 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT MOD_RES 623 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" SQ SEQUENCE 730 AA; 78349 MW; 736DFBBC637F8026 CRC64; MTERTTRHSL QVATELYRFI EDKVLPGTGV DSDKFWSGFD AIVADLAPKN IALLAERDRL QLEMDAWHKA NPGPIADMPA YRAFLESIGY LVPQPETVAV TTANVDAELA VQAGPQLVVP VLNARYALNA ANARWGSLYD ALYGTDAIPE TDGAEKGKGY NPVRGAKVIA FARNLLDQAA PLSTGSHKDA TGYSIEGGQL VVTQASGMSG LQDPAQLVGY RGDAAAPSSV LLVHNGLHID IIIDRATTLG KSDAAGISDM VIESALSTIL DLEDSVAVVD AEDKVLAYGN WLGILQGTLT EEVSKGGTTF TRGLNPDRVY TAADGGEVTL HGRSLMFVRN VGHLMTNPAI LYAGGKEIPE GIMDAVVTTT IAIHDFKRQG QPGIKNSRTG SVYIVKPKMH GPAEVAFAAE LFGRVEALLG LPANTVKLGI MDEERRTSVN LKACIAEAEA RVAFINTGFL DRTGDEMHTA MQAGPMIRKG DMKTSAWIAA YEKNNVLVGL SCGLRGKAQI GKGMWAMPDL MAAMLEQKIG HPKAGANTAW VPSPTAATLH ALHYHQVLVS DVQKELEKID ANAERGNLLN GLLQIPVTAT PNWSDAEKQQ ELDNNAQGIL GYVVRWIDQG VGCSKVPDIH NIALMEDRAT LRISSQHMAN WLHHGVVTEA QVKETFERMA AVVDGQNAGD PLYKNMAGHF DTSAAYKAAC DLVFKGLEQP SGYTEPLLHA WRLKVKAGTA //